The overall goals of the research are to develop methods for describing the structure and dynamics of biopolymers that are integral parts of supramolecular structures and to apply these methods to the study of the filamentous bacteriophages. A direct consequence of the research support by this grant is that solid- state NMR spectroscopy is now on the verge of joining x-ray diffraction and solution NMR spectroscopy as a third independent method for determining the structures of proteins at atomic resolution, including proteins in nucleoprotein or membrane-protein complexes. These systems are difficult or impossible to study by x-ray diffraction, because of its requirements for single crystal samples, or solution NMR spectroscopy, because of its requirements for low molecular weight and rapidly reorienting samples. The emphasis of the research is on proteins, however these methods are applicable to nucleic acids, and are related to methods appropriate for lipids and carbohydrates. Most of the current research utilizes oriented systems in the structural studies; this approach will continue, however several methods for obtaining structural information form spectroscopy is highly effective at describing the intramolecular motions of proteins and will be used to analyze both backbone and sidechain motions over the range of timescales from 102 to 1010 Hz.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
5R01GM024266-15
Application #
3272161
Study Section
Biophysical Chemistry Study Section (BBCB)
Project Start
1977-08-01
Project End
1993-07-31
Budget Start
1991-08-01
Budget End
1992-07-31
Support Year
15
Fiscal Year
1991
Total Cost
Indirect Cost
Name
University of Pennsylvania
Department
Type
Schools of Arts and Sciences
DUNS #
042250712
City
Philadelphia
State
PA
Country
United States
Zip Code
19104
Rosay, M; Zeri, A C; Astrof, N S et al. (2001) Sensitivity-enhanced NMR of biological solids: dynamic nuclear polarization of Y21M fd bacteriophage and purple membrane. J Am Chem Soc 123:1010-1
Ramamoorthy, A; Opella, S J (1995) Two-dimensional chemical shift/heteronuclear dipolar coupling spectra obtained with polarization inversion spin exchange at the magic angle and magic-angle sample spinning (PISEMAMAS). Solid State Nucl Magn Reson 4:387-92
Ramamoorthy, A; Wu, C H; Opella, S J (1995) Three-dimensional solid-state NMR experiment that correlates the chemical shift and dipolar coupling frequencies of two heteronuclei. J Magn Reson B 107:88-90
Opella, S J (1994) Solid-state NMR structural studies of proteins. Annu Rev Phys Chem 45:659-83
Opella, S J; Kim, Y; McDonnell, P (1994) Experimental nuclear magnetic resonance studies of membrane proteins. Methods Enzymol 239:536-60
Bechinger, B; Zasloff, M; Opella, S J (1993) Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy. Protein Sci 2:2077-84
McDonnell, P A; Shon, K; Kim, Y et al. (1993) fd coat protein structure in membrane environments. J Mol Biol 233:447-63
Bechinger, B; Zasloff, M; Opella, S J (1992) Structure and interactions of magainin antibiotic peptides in lipid bilayers: a solid-state nuclear magnetic resonance investigation. Biophys J 62:12-4
Bechinger, B; Kim, Y; Chirlian, L E et al. (1991) Orientations of amphipathic helical peptides in membrane bilayers determined by solid-state NMR spectroscopy. J Biomol NMR 1:167-73
Opella, S J; Stewart, P L (1989) Solid-state nuclear magnetic resonance structural studies of proteins. Methods Enzymol 176:242-75

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